Activation of Pyrococcus furiosus alkaline phosphatase by divalent metal ions

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Treatment of a hyperthermophilic enzyme, alkaline phosphatase from Pyrococcus furiosus (PfuAP), with EDTA completely deactivated PfuAP, indicating that the presence of one or more divalent metal ions is essential for its catalytic activity. Subsequent addition of various divalent metal ions to the apoprotein recovered the enzymatic activity and, in particular, the addition of Co(II) resulted in an over 50-fold increase in activity compared with PfuAP before EDTA treatment. Intriguingly, PfuAP with Co(II) exhibited weaker stability toward heat treatment, suggesting that Co2+ destabilizes the tertiary structure of PfuAP at high temperature.

Original languageEnglish
Pages (from-to)2055-2060
Number of pages6
JournalBiotechnology letters
Volume34
Issue number11
DOIs
Publication statusPublished - Oct 1 2012

    Fingerprint

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

Cite this